EMC9_MOUSE
ID EMC9_MOUSE Reviewed; 206 AA.
AC Q9DB76;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ER membrane protein complex subunit 9;
DE AltName: Full=Protein FAM158A;
GN Name=Emc9; Synonyms=Cgi112, Fam158a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex
CC (EMC) that enables the energy-independent insertion into endoplasmic
CC reticulum membranes of newly synthesized membrane proteins.
CC Preferentially accommodates proteins with transmembrane domains that
CC are weakly hydrophobic or contain destabilizing features such as
CC charged and aromatic residues. Involved in the cotranslational
CC insertion of multi-pass membrane proteins in which stop-transfer
CC membrane-anchor sequences become ER membrane spanning helices. It is
CC also required for the post-translational insertion of tail-anchored/TA
CC proteins in endoplasmic reticulum membranes. By mediating the proper
CC cotranslational insertion of N-terminal transmembrane domains in an N-
CC exo topology, with translocated N-terminus in the lumen of the ER,
CC controls the topology of multi-pass membrane proteins like the G
CC protein-coupled receptors. By regulating the insertion of various
CC proteins in membranes, it is indirectly involved in many cellular
CC processes. {ECO:0000250|UniProtKB:Q9Y3B6}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC). EMC8 and
CC EMC9 are mutually exclusive subunits of the EMC complex.
CC {ECO:0000250|UniProtKB:Q9Y3B6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y3B6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y3B6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Y3B6}.
CC -!- SIMILARITY: Belongs to the EMC8/EMC9 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK005154; BAB23847.1; -; mRNA.
DR EMBL; BC024704; AAH24704.1; -; mRNA.
DR CCDS; CCDS27117.1; -.
DR RefSeq; NP_149158.1; NM_033146.1.
DR AlphaFoldDB; Q9DB76; -.
DR SMR; Q9DB76; -.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR STRING; 10090.ENSMUSP00000022828; -.
DR PhosphoSitePlus; Q9DB76; -.
DR MaxQB; Q9DB76; -.
DR PaxDb; Q9DB76; -.
DR PRIDE; Q9DB76; -.
DR ProteomicsDB; 275613; -.
DR Antibodypedia; 55830; 50 antibodies from 13 providers.
DR DNASU; 85308; -.
DR Ensembl; ENSMUST00000022828; ENSMUSP00000022828; ENSMUSG00000022217.
DR GeneID; 85308; -.
DR KEGG; mmu:85308; -.
DR UCSC; uc007tze.1; mouse.
DR CTD; 51016; -.
DR MGI; MGI:1934682; Emc9.
DR VEuPathDB; HostDB:ENSMUSG00000022217; -.
DR eggNOG; KOG3289; Eukaryota.
DR GeneTree; ENSGT00390000006738; -.
DR HOGENOM; CLU_087337_0_1_1; -.
DR InParanoid; Q9DB76; -.
DR OMA; QANACAS; -.
DR OrthoDB; 1284861at2759; -.
DR PhylomeDB; Q9DB76; -.
DR TreeFam; TF313860; -.
DR BioGRID-ORCS; 85308; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9DB76; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9DB76; protein.
DR Bgee; ENSMUSG00000022217; Expressed in facial nucleus and 203 other tissues.
DR ExpressionAtlas; Q9DB76; baseline and differential.
DR Genevisible; Q9DB76; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; ISS:UniProtKB.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR CDD; cd08060; MPN_UPF0172; 1.
DR InterPro; IPR005366; EMC8/9.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR12941; PTHR12941; 1.
DR Pfam; PF03665; UPF0172; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome.
FT CHAIN 1..206
FT /note="ER membrane protein complex subunit 9"
FT /id="PRO_0000221190"
FT DOMAIN 4..139
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 206 AA; 22787 MW; 5A189C0AF8B20126 CRC64;
MGEVEISARA YGKMCLHASR YPHAAVNGLL LAPATGSGEC LCLTDCVPLF HSHLALSVML
EVALNQVDVW GAQAGLVVAG YYHANAVLDD QSPGPLALKI AGRIAEFFPR AVLIMLDNKK
LVTRPRVPPV IVLENQGLQW VPKDKNLVMW RDWEESRQMV GALLEGRAHQ HLVDFDCHLD
DIRQDWTNQR LNTQITQWSG STDGNA
